GPI8_HUMAN - dbPTM
GPI8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPI8_HUMAN
UniProt AC Q92643
Protein Name GPI-anchor transamidase
Gene Name PIGK
Organism Homo sapiens (Human).
Sequence Length 395
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein .
Protein Description Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein..
Protein Sequence MAVTDSLSRAATVLATVLLLSFGSVAASHIEDQAEQFFRSGHTNNWAVLVCTSRFWFNYRHVANTLSVYRSVKRLGIPDSHIVLMLADDMACNPRNPKPATVFSHKNMELNVYGDDVEVDYRSYEVTVENFLRVLTGRIPPSTPRSKRLLSDDRSNILIYMTGHGGNGFLKFQDSEEITNIELADAFEQMWQKRRYNELLFIIDTCQGASMYERFYSPNIMALASSQVGEDSLSHQPDPAIGVHLMDRYTFYVLEFLEEINPASQTNMNDLFQVCPKSLCVSTPGHRTDLFQRDPKNVLITDFFGSVRKVEITTETIKLQQDSEIMESSYKEDQMDEKLMEPLKYAEQLPVAQIIHQKPKLKDWHPPGGFILGLWALIIMVFFKTYGIKHMKFIF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
67PhosphorylationRHVANTLSVYRSVKR
HHHHHHHHHHHHHHH
18.3124719451
69PhosphorylationVANTLSVYRSVKRLG
HHHHHHHHHHHHHHC
8.19-
98UbiquitinationACNPRNPKPATVFSH
CCCCCCCCCCEECEE
51.3221963094
106UbiquitinationPATVFSHKNMELNVY
CCEECEECCEEEEEE
57.7121963094
142PhosphorylationLTGRIPPSTPRSKRL
HHCCCCCCCCCHHHC
45.7728188228
143PhosphorylationTGRIPPSTPRSKRLL
HCCCCCCCCCHHHCC
28.6123403867
151PhosphorylationPRSKRLLSDDRSNIL
CCHHHCCCCCCCCEE
41.9024719451
155PhosphorylationRLLSDDRSNILIYMT
HCCCCCCCCEEEEEE
34.9128348404
193UbiquitinationAFEQMWQKRRYNELL
HHHHHHHHHCCCCEE
24.2721906983
212PhosphorylationTCQGASMYERFYSPN
CCCCHHHHHHHHCCC
11.06-
216PhosphorylationASMYERFYSPNIMAL
HHHHHHHHCCCCHHH
29.4620860994
225PhosphorylationPNIMALASSQVGEDS
CCCHHHHHCCCCCCH
23.3520860994
296UbiquitinationDLFQRDPKNVLITDF
CHHHCCCCCEEEEEC
65.0721906983
2962-HydroxyisobutyrylationDLFQRDPKNVLITDF
CHHHCCCCCEEEEEC
65.07-
301PhosphorylationDPKNVLITDFFGSVR
CCCCEEEEECCCCEE
23.69-
306PhosphorylationLITDFFGSVRKVEIT
EEEECCCCEEEEEEE
17.37-
309UbiquitinationDFFGSVRKVEITTET
ECCCCEEEEEEEECE
41.9016196087
314O-linked_GlycosylationVRKVEITTETIKLQQ
EEEEEEEECEEEHHH
36.47OGP
318UbiquitinationEITTETIKLQQDSEI
EEEECEEEHHHCHHH
47.8921963094
331UbiquitinationEIMESSYKEDQMDEK
HHHHHCCCHHHHCHH
57.6821906983
344UbiquitinationEKLMEPLKYAEQLPV
HHHHHHHHHHHHCCH
53.8021963094
358UbiquitinationVAQIIHQKPKLKDWH
HHHHHCCCCCCCCCC
29.9221906983
360UbiquitinationQIIHQKPKLKDWHPP
HHHCCCCCCCCCCCC
75.1822817900
362UbiquitinationIHQKPKLKDWHPPGG
HCCCCCCCCCCCCCH
65.9722817900

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of GPI8_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPI8_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GPI8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PIGT_HUMANPIGTphysical
12582175
CALX_HUMANCANXphysical
12582175
ULBP2_HUMANULBP2physical
12582175
PPB1_HUMANALPPphysical
11278620
GPAA1_HUMANGPAA1physical
10793132
GPAA1_HUMANGPAA1physical
12052837
PIGT_HUMANPIGTphysical
22939629
PIGS_HUMANPIGSphysical
22939629
PIGU_HUMANPIGUphysical
22939629
PIGT_HUMANPIGTphysical
26186194
GPAA1_HUMANGPAA1physical
26186194
PIGS_HUMANPIGSphysical
26186194
PIGU_HUMANPIGUphysical
26186194
GPAA1_HUMANGPAA1physical
28514442
PIGU_HUMANPIGUphysical
28514442
PIGT_HUMANPIGTphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPI8_HUMAN

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Related Literatures of Post-Translational Modification

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